5DJ9
Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with gabaculine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-04-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 56.258, 60.887, 63.499 |
| Unit cell angles | 100.83, 92.38, 107.86 |
Refinement procedure
| Resolution | 30.000 - 1.550 |
| R-factor | 0.15963 |
| Rwork | 0.158 |
| R-free | 0.19031 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.691 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHENIX |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.060 | 0.550 |
| Number of reflections | 109959 | |
| <I/σ(I)> | 20.6 | 3.2 |
| Completeness [%] | 96.5 | 94.7 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 292 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350, 5mM gabaculine and 2mM PLP |
